ID A0A418WC94_9PROT Unreviewed; 417 AA.
AC A0A418WC94;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=L-serine dehydratase {ECO:0000256|ARBA:ARBA00031418};
DE EC=4.3.1.17 {ECO:0000256|ARBA:ARBA00012093};
DE EC=4.3.1.19 {ECO:0000256|ARBA:ARBA00012096};
GN ORFNames=D3874_11950 {ECO:0000313|EMBL:RJF87645.1};
OS Oleomonas cavernae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Oleomonas.
OX NCBI_TaxID=2320859 {ECO:0000313|EMBL:RJF87645.1, ECO:0000313|Proteomes:UP000284605};
RN [1] {ECO:0000313|EMBL:RJF87645.1, ECO:0000313|Proteomes:UP000284605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K1W22B-8 {ECO:0000313|EMBL:RJF87645.1,
RC ECO:0000313|Proteomes:UP000284605};
RA Zhu H.;
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the anaerobic formation of alpha-ketobutyrate and
CC ammonia from threonine in a two-step reaction. The first step involved
CC a dehydration of threonine and a production of enamine intermediates
CC (aminocrotonate), which tautomerizes to its imine form (iminobutyrate).
CC Both intermediates are unstable and short-lived. The second step is the
CC nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-
CC ketobutyrate and free ammonia. In the low water environment of the
CC cell, the second step is accelerated by RidA. TdcB also dehydrates
CC serine to yield pyruvate via analogous enamine/imine intermediates.
CC {ECO:0000256|ARBA:ARBA00025594}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from L-threonine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004810}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RJF87645.1}.
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DR EMBL; QYUK01000011; RJF87645.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418WC94; -.
DR OrthoDB; 9811476at2; -.
DR UniPathway; UPA00047; UER00054.
DR Proteomes; UP000284605; Unassembled WGS sequence.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006567; P:threonine catabolic process; IEA:InterPro.
DR CDD; cd04886; ACT_ThrD-II-like; 1.
DR CDD; cd01562; Thr-dehyd; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR044561; ACT_ThrD-II-like.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR005789; Thr_deHydtase_catblc.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01127; ilvA_1Cterm; 1.
DR PANTHER; PTHR48078:SF6; ACT DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF13291; ACT_4; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624};
KW Lyase {ECO:0000313|EMBL:RJF87645.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000284605}.
FT DOMAIN 336..415
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 417 AA; 43772 MW; F5F2FF297C125C71 CRC64;
MTSLAPIPAP LPVTIDDVRQ AAANLRGQIV ETPTAFSRTL SQVTGARVHL KFENQQFTAS
FKDRGACYKL QSLSEAERRA GVIAVSAGNH AQGVAYHAAR LGIPATIVMP RNTPFVKVRQ
TREHGARVVL EGEILSESFA AAKRIGAAEG LMLIHPFDDT RIIAGQGTVA LEMLAEFPDL
DCLVVPIGGG GLIAGVAIAA KAHNPGIEII GVETALYPSM YHAMRGEPAQ CGGATIAEGI
AVKDAGQITL AICRELVAEI MLVSDADLER AIGLLLAIEK TVVEGAGAAG LAALLANPQR
FSGKRVGLVL TGGNIDPRLL GEVIRRNLVR EGRIAGLRVM ISDSPGTLAK IASLIGEGGG
NILEVSHQRL FLDVPVKNAD LDLVVETRDA AHLDEIIASI TTAGYPVRRL RSTDAAG
//
